SLYA_CALRH
ID SLYA_CALRH Reviewed; 136 AA.
AC Q9I841;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Snaclec rhodocytin subunit alpha;
DE AltName: Full=Aggretin alpha chain;
DE AltName: Full=Rhodoaggretin subunit alpha;
OS Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Calloselasma.
OX NCBI_TaxID=8717;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-22.
RC TISSUE=Venom, and Venom gland;
RX PubMed=10512747; DOI=10.1006/bbrc.1999.1457;
RA Chung C.-H., Au L.-C., Huang T.-F.;
RT "Molecular cloning and sequence analysis of aggretin, a collagen-like
RT platelet aggregation inducer.";
RL Biochem. Biophys. Res. Commun. 263:723-727(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-30, AND FUNCTION.
RX PubMed=11287424; DOI=10.1074/jbc.m101585200;
RA Navdaev A., Clemetson J.M., Polgar J., Kehrel B.E., Glauner M.,
RA Magnenat E., Wells T.N.C., Clemetson K.J.;
RT "Aggretin, a heterodimeric C-type lectin from Calloselasma rhodostoma
RT (malayan pit viper), stimulates platelets by binding to alpha 2beta 1
RT integrin and glycoprotein Ib, activating Syk and phospholipase Cgamma 2,
RT but does not involve the glycoprotein VI/Fc receptor gamma chain collagen
RT receptor.";
RL J. Biol. Chem. 276:20882-20889(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-22, FUNCTION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=9588185; DOI=10.1006/bbrc.1998.8516;
RA Shin Y., Morita T.;
RT "Rhodocytin, a functional novel platelet agonist belonging to the
RT heterodimeric C-type lectin family, induces platelet aggregation
RT independently of glycoprotein Ib.";
RL Biochem. Biophys. Res. Commun. 245:741-745(1998).
RN [4]
RP PROTEIN SEQUENCE OF 1-22, FUNCTION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=11728470; DOI=10.1016/s0014-5793(01)03071-x;
RA Wang R., Kong C., Kolatkar P., Chung M.C.;
RT "A novel dimer of a C-type lectin-like heterodimer from the venom of
RT Calloselasma rhodostoma (Malayan pit viper).";
RL FEBS Lett. 508:447-453(2001).
RN [5]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=7639679; DOI=10.1042/bj3091021;
RA Huang T.-F., Liu C.-Z., Yang S.-H.;
RT "Aggretin, a novel platelet-aggregation inducer from snake (Calloselasma
RT rhodostoma) venom, activates phospholipase C by acting as a glycoprotein
RT Ia/IIa agonist.";
RL Biochem. J. 309:1021-1027(1995).
RN [6]
RP FUNCTION.
RX PubMed=11453648; DOI=10.1006/bbrc.2001.5228;
RA Chung C.-H., Peng H.-C., Huang T.-F.;
RT "Aggretin, a C-type lectin protein, induces platelet aggregation via
RT integrin alpha(2)beta(1) and GPIb in a phosphatidylinositol 3-kinase
RT independent pathway.";
RL Biochem. Biophys. Res. Commun. 285:689-695(2001).
RN [7]
RP FUNCTION.
RX PubMed=11352922; DOI=10.1074/jbc.m103892200;
RA Bergmeier W., Bouvard D., Eble J.A., Mokhtari-Nejad R., Schulte V.,
RA Zirngibl H., Brakebusch C., Fassler R., Nieswandt B.;
RT "Rhodocytin (aggretin) activates platelets lacking alpha(2)beta(1)
RT integrin, glycoprotein VI, and the ligand-binding domain of glycoprotein
RT Ibalpha.";
RL J. Biol. Chem. 276:25121-25126(2001).
RN [8]
RP FUNCTION.
RX PubMed=14630793; DOI=10.1182/blood-2003-07-2483;
RA Chung C.-H., Wu W.-B., Huang T.-F.;
RT "Aggretin, a snake venom-derived endothelial integrin alpha 2 beta 1
RT agonist, induces angiogenesis via expression of vascular endothelial growth
RT factor.";
RL Blood 103:2105-2113(2004).
RN [9]
RP FUNCTION.
RX PubMed=16174766; DOI=10.1182/blood-2005-05-1994;
RA Suzuki-Inoue K., Fuller G.L.J., Garcia A., Eble J.A., Poehlmann S.,
RA Inoue O., Gartner T.K., Hughan S.C., Pearce A.C., Laing G.D.,
RA Theakston R.D.G., Schweighoffer E., Zitzmann N., Morita T.,
RA Tybulewicz V.L.J., Ozaki Y., Watson S.P.;
RT "A novel Syk-dependent mechanism of platelet activation by the C-type
RT lectin receptor CLEC-2.";
RL Blood 107:542-549(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=18597489; DOI=10.1021/bi800528t;
RA Hooley E., Papagrigoriou E., Navdaev A., Pandey A.V., Clemetson J.M.,
RA Clemetson K.J., Emsley J.;
RT "The crystal structure of the platelet activator aggretin reveals a novel
RT (alphabeta)2 dimeric structure.";
RL Biochemistry 47:7831-7837(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS), SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=18583525; DOI=10.1110/ps.035568.108;
RA Watson A.A., Eble J.A., O'Callaghan C.A.;
RT "Crystal structure of rhodocytin, a ligand for the platelet-activating
RT receptor CLEC-2.";
RL Protein Sci. 17:1611-1616(2008).
CC -!- FUNCTION: Elicits platelet aggregation by the binding to the C-type
CC lectin domain family 1 member B (CLEC1B/CLEC2). Binding leads to
CC tyrosine phosphorylation in the cytoplasmic tail of CLEC1B, which
CC promotes the binding of spleen tyrosine kinase (Syk), subsequent
CC activation of PLC-gamma-2, and platelet activation and aggregation.
CC Binding to GPIbalpha (GP1BA) and alpha-2/beta-1 (ITGA2/ITGB1) may also
CC induce aggregation, but this is controversial.
CC {ECO:0000269|PubMed:11287424, ECO:0000269|PubMed:11352922,
CC ECO:0000269|PubMed:11453648, ECO:0000269|PubMed:11728470,
CC ECO:0000269|PubMed:14630793, ECO:0000269|PubMed:16174766,
CC ECO:0000269|PubMed:7639679, ECO:0000269|PubMed:9588185}.
CC -!- SUBUNIT: Dimer (non-covalently linked) of heterodimers of subunits
CC alpha and beta (disulfide-linked). {ECO:0000269|PubMed:11728470,
CC ECO:0000269|PubMed:18583525, ECO:0000269|PubMed:18597489,
CC ECO:0000269|PubMed:9588185}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; AF244900; AAF79952.1; -; mRNA.
DR PIR; PC7027; PC7027.
DR PDB; 2VRP; X-ray; 2.41 A; A=1-136.
DR PDB; 3BX4; X-ray; 1.70 A; A/C=1-136.
DR PDB; 3WWK; X-ray; 2.98 A; A/D/G/J=1-136.
DR PDBsum; 2VRP; -.
DR PDBsum; 3BX4; -.
DR PDBsum; 3WWK; -.
DR AlphaFoldDB; Q9I841; -.
DR SMR; Q9I841; -.
DR DIP; DIP-61334N; -.
DR IntAct; Q9I841; 1.
DR EvolutionaryTrace; Q9I841; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0060300; P:regulation of cytokine activity; IDA:CACAO.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Metal-binding;
KW Platelet aggregation activating toxin; Secreted; Toxin.
FT CHAIN 1..136
FT /note="Snaclec rhodocytin subunit alpha"
FT /id="PRO_0000355238"
FT DOMAIN 12..132
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 5..16
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 33..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 83
FT /note="Interchain (with C-98 in beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:18583525, ECO:0000269|PubMed:18597489"
FT DISULFID 106..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:3BX4"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:3BX4"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:3BX4"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:3BX4"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:3BX4"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3BX4"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3BX4"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:3BX4"
SQ SEQUENCE 136 AA; 15796 MW; 3B474A4149F0027A CRC64;
GLEDCDFGWS PYDQHCYQAF NEQKTWDEAE KFCRAQENGA HLASIESNGE ADFVSWLISQ
KDELADEDYV WIGLRAQNKE QQCSSEWSDG SSVSYENLID LHTKKCGALE KLTGFRKWVN
YYCEQMHAFV CKLLPY
